Literature summary for 2.3.2.26 extracted from

Wang, Z.; Liu, Z.; Chen, X.; Li, J.; Yao, W.; Huang, S.; Gu, A.; Lei, Q.; Mao, Y.; Wen, W.
A multi-lock inhibitory mechanism for fine-tuning enzyme activities of the HECT family E3 ligases (2019), Nat. Commun., 10, 3162 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of WWP1 in its fully inactive and partially active states. Domains WW2, L, and WW4 are organized into a headset architecture, in which the WW2 and WW4 domains are bound to bilateral sites within the N-lobe, and L forms a kinked alpha-helix that is tucked into the cleft between the N- and C-lobes of HECT	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
medicine	many WWP1 mutations identified in cancer patients result in a partially active state with increased E3 ligase activity, and the WWP1 mutants likely promote cell migration by enhancement of DELTANp63alpha degradation	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9H0M0	isoform WWP1	-

Synonyms

Synonyms	Comment	Organism
WWP1	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	HECT E3 ligase adopts an autoinhibited state, in which its multiple WW domains sequester HECT using a multi-lock mechanism. Removing WW2 or WW34 leads to a partial activation of WWP1. The multi-lock regulation mechanism is conserved in WWP2 and Itch, whereas in Nedd4/4 L and Smurf2, a variant version of the multi-lock autoinhibition mode is utilized	Homo sapiens

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Release 2023.1 (January 2023)